4f2e | pdb_00004f2e

Crystal structure of the Streptococcus pneumoniae D39 copper chaperone CupA with Cu(I)

spinqualitylabelsall models 4f2e, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f2e is a 1 chain structure with sequence from Streptococcus pneumoniae D39. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, CU1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2ZPL4_STRP2 Publication Abstract from PubMed Copper resistance has emerged as an important virulence determinant of microbial pathogens. In Streptococcus pneumoniae, copper resistance is mediated by the copper-responsive repressor CopY, CupA and the copper-effluxing P(1B)-type ATPase CopA. We show here that CupA is a previously uncharacterized cell membrane-anchored Cu(I) chaperone and that a Cu(I) binding-competent, membrane-localized CupA is obligatory for copper resistance. The crystal structures of the soluble domain of CupA and the N-terminal metal-binding domain (MBD) of CopA (CopA(MBD)) reveal isostructural cupredoxin-like folds that each harbor a binuclear Cu(I) cluster unprecedented in bacterial copper trafficking. NMR studies reveal unidirectional Cu(I) transfer from the low-affinity site on the soluble domain of CupA to the high-affinity site of CopA(MBD). However, copper binding by CopA(MBD) is not essential for cellular copper resistance, consistent with a primary role of CupA in cytoplasmic Cu(I) sequestration and/or direct delivery to the transmembrane site of CopA for cellular efflux. A new structural paradigm in copper resistance in Streptococcus pneumoniae.,Fu Y, Tsui HC, Bruce KE, Sham LT, Higgins KA, Lisher JP, Kazmierczak KM, Maroney MJ, Dann CE 3rd, Winkler ME, Giedroc DP Nat Chem Biol. 2013 Jan 27. doi: 10.1038/nchembio.1168. PMID:23354287 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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